About: Bat IFITM3 restriction depends on S-palmitoylation and a polymorphic site within the CD225 domain

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About: Bat IFITM3 restriction depends on S-palmitoylation and a polymorphic site within the CD225 domain Goto Sponge NotDistinct Permalink

An Entity of Type : schema:ScholarlyArticle, within Data Space : wasabi.inria.fr associated with source document(s)

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type	Academic Article research paper schema:ScholarlyArticle
isDefinedBy	Covid-on-the-Web dataset
has title	Bat IFITM3 restriction depends on S-palmitoylation and a polymorphic site within the CD225 domain
Creator	Kellam, Paul Marsh, Mark Weston, Stuart Mazzon, Michela Ritzefeld, Markus Tate, Edward Holmes, Edward Mackenzie, Farrell Smith, Sarah Teo, Han To Benfield, Camilla
topic	covid:a57080f174e3ede5138af08070a2b9db8f9c36a7#this
Source	Medline; PMC
abstract	Host interferon-induced transmembrane proteins (IFITMs) are broad-spectrum antiviral restriction factors. Of these, IFITM3 potently inhibits viruses that enter cells through acidic endosomes, many of which are zoonotic and emerging viruses with bats (order Chiroptera) as their natural hosts. We previously demonstrated that microbat IFITM3 is antiviral. Here, we show that bat IFITMs are characterized by strong adaptive evolution and identify a highly variable and functionally important site—codon 70—within the conserved CD225 domain of IFITMs. Mutation of this residue in microbat IFITM3 impairs restriction of representatives of four different virus families that enter cells via endosomes. This mutant shows altered subcellular localization and reduced S-palmitoylation, a phenotype copied by mutation of conserved cysteine residues in microbat IFITM3. Furthermore, we show that microbat IFITM3 is S-palmitoylated on cysteine residues C71, C72, and C105, mutation of each cysteine individually impairs virus restriction, and a triple C71A-C72A-C105A mutant loses all restriction activity, concomitant with subcellular re-localization of microbat IFITM3 to Golgi-associated sites. Thus, we propose that S-palmitoylation is critical for Chiropteran IFITM3 function and identify a key molecular determinant of IFITM3 S-palmitoylation.
has issue date	2019-12-11(xsd:dateTime)
bibo:doi	10.26508/lsa.201900542
bibo:pmid	31826928
has license	cc-by
sha1sum (hex)	a57080f174e3ede5138af08070a2b9db8f9c36a7
schema:url	https://doi.org/10.26508/lsa.201900542
resource representing a document's title	Bat IFITM3 restriction depends on S-palmitoylation and a polymorphic site within the CD225 domain
has PubMed Central identifier	PMC6907390
has PubMed identifier	31826928
schema:publication	Life Sci Alliance
resource representing a document's body	covid:a57080f174e3ede5138af08070a2b9db8f9c36a7#body_text
is http://vocab.deri.ie/void#inDataset of	proxy:http/ns.inria.fr/covid19/a57080f174e3ede5138af08070a2b9db8f9c36a7
is schema:about of	named entity 'S-PALMITOYLATION' named entity 'POLYMORPHIC SITE' named entity 'CD225' named entity 'DOMAIN' named entity 'DIFFERENT' named entity 'THESE' named entity 'BATS' named entity 'C72' named entity 'ENTER' named entity 'CELLS' named entity 'CONSERVED' named entity 'PREVIOUSLY' named entity 'RESTRICTION' named entity 'HOST' named entity 'ENDOSOMES' named entity 'GOLGI' named entity 'ANTIVIRAL' named entity 'MOLECULAR' named entity 'THEIR' named entity 'KEY' named entity 'BAT' named entity 'CRITICAL' named entity 'ACIDIC' named entity 'ALTERED' named entity 'MUTANT' named entity 'FUNCTION' named entity 'CYSTEINE' named entity 'MUTATION' named entity 'ZOONOTIC' named entity 'VIRUS' named entity 'HIGHLY' named entity 'DEMONSTRATED' named entity 'IMPORTANT' named entity 'STRONG' named entity 'ACTIVITY' named entity 'SPECTRUM' named entity 'BROAD' named entity 'PHENOTYPE' named entity 'OF EACH' named entity 'ADAPTIVE EVOLUTION' named entity 'IFITM3' named entity 'ASSOCIATED' named entity 'CHARACTERIZED' named entity 'FAMILIES' named entity 'IFITM3' named entity 'INTERFERON' named entity 'RESTRICTION' named entity 'BAT' named entity 'TRIPLE' named entity 'IMPAIRS' named entity 'C71' named entity 'SITE' named entity 'LOCALIZATION' named entity 'DOMAIN' named entity 'PALMITOYLATED' named entity 'CODON' named entity 'DETERMINANT' named entity 'INDUCED' named entity 'REDUCED' named entity 'VARIABLE' named entity 'CD225' named entity 'CONCOMITANT' named entity 'TRANSMEMBRANE PROTEINS' named entity 'CHIROPTERA' named entity 'IDENTIFY' named entity 'HERE' named entity 'RESIDUE' named entity 'S-PALMITOYLATION' named entity 'NATURAL'

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